Document Detail


FHOD proteins in actin dynamics - a formin' class of its own.
MedLine Citation:
PMID:  25483300     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Abstract Eukaryotic cells have evolved a variety of actin-binding proteins to regulate the architecture and the dynamics of the actin cytoskeleton in time and space. The Diaphanous-related formins (DRF) represent a diverse group of Rho-GTPase-regulated actin regulators that control a range of actin structures composed of tightly-bundled, unbranched actin filaments as found in stress fibers and in filopodia. Under resting conditions, DRFs are auto-inhibited by an intra-molecular interaction between the C-terminal and the N-terminal domains. The auto-inhibition is thought to be released by binding of an activated RhoGTPase to the N-terminal GTPase-binding domain (GBD). However, there is growing evidence for more sophisticated variations from this simplified linear activation model. In this review we focus on the formin homology domain-containing proteins (FHOD), an unconventional group of DRFs. Recent findings on the molecular control and cellular functions of FHOD proteins in vivo are discussed in the light of the phylogeny of FHOD proteins.
Authors:
Meike Bechtold; Jörg Schultz; Sven Bogdan
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-11-14
Journal Detail:
Title:  Small GTPases     Volume:  -     ISSN:  2154-1256     ISO Abbreviation:  Small GTPases     Publication Date:  2014 Nov 
Date Detail:
Created Date:  2014-12-8     Completed Date:  -     Revised Date:  2014-12-9    
Medline Journal Info:
Nlm Unique ID:  101530974     Medline TA:  Small GTPases     Country:  -    
Other Details:
Languages:  ENG     Pagination:  0     Citation Subset:  -    
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